17892531

Source:http://linkedlifedata.com/resource/pubmed/id/17892531

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0032173, umls-concept:C0041485, umls-concept:C0086418, umls-concept:C0917705
pubmed:issue	12
pubmed:dateCreated	2007-11-23
pubmed:abstractText	Canonical transient receptor potential channels (TRPCs), which are regulated by several processes, including tyrosine phosphorylation, are candidates for the conduction of store-operated Ca(2+) entry (SOCE).
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/064070
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101170508
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Actinin, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes, http://linkedlifedata.com/resource/pubmed/chemical/NSC-87877, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase..., http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Quinolines, http://linkedlifedata.com/resource/pubmed/chemical/STIM1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/TRPC Cation Channels, http://linkedlifedata.com/resource/pubmed/chemical/TRPC4 ion channel, http://linkedlifedata.com/resource/pubmed/chemical/TRPC5 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Thrombin, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine, http://linkedlifedata.com/resource/pubmed/chemical/transient receptor potential...
pubmed:status	MEDLINE
pubmed:month	Dec
pubmed:issn	1538-7933
pubmed:author	pubmed-author:BrownlowS LSL, pubmed-author:HarperA G SAG, pubmed-author:HarpinM LML, pubmed-author:RedondoP CPC, pubmed-author:RosadoJ AJA, pubmed-author:SageS OSO
pubmed:issnType	Print
pubmed:volume	5
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	2476-83
pubmed:dateRevised	2009-11-19
pubmed:meshHeading	pubmed-meshheading:17892531-Actinin, pubmed-meshheading:17892531-Blood Platelets, pubmed-meshheading:17892531-Blotting, Western, pubmed-meshheading:17892531-Calcium Signaling, pubmed-meshheading:17892531-Enzyme Inhibitors, pubmed-meshheading:17892531-Humans, pubmed-meshheading:17892531-Immunoprecipitation, pubmed-meshheading:17892531-Membrane Proteins, pubmed-meshheading:17892531-Multiprotein Complexes, pubmed-meshheading:17892531-Neoplasm Proteins, pubmed-meshheading:17892531-Phosphorylation, pubmed-meshheading:17892531-Phosphotyrosine, pubmed-meshheading:17892531-Platelet Activation, pubmed-meshheading:17892531-Protein Tyrosine Phosphatase, Non-Receptor Type 6, pubmed-meshheading:17892531-Protein-Tyrosine Kinases, pubmed-meshheading:17892531-Quinolines, pubmed-meshheading:17892531-TRPC Cation Channels, pubmed-meshheading:17892531-Thrombin, pubmed-meshheading:17892531-Time Factors, pubmed-meshheading:17892531-Tyrosine
pubmed:year	2007
pubmed:articleTitle	hTRPC1-associated alpha-actinin, and not hTRPC1 itself, is tyrosine phosphorylated during human platelet activation.
pubmed:affiliation	Department of Physiology, Development and Neuroscience, University of Cambridge, Cambridge, UK.
pubmed:publicationType	Journal Article, In Vitro, Research Support, Non-U.S. Gov't